The mechanism of bacterial infection by filamentous phages involves molecular interactions between TolA and phage protein 3 domains
(2003) In Journal of Bacteriology 185(8). p.2628-2634- Abstract
- The early events in filamentous bacteriophage infection of gram-negative bacteria are mediated by the gene 3 protein (g3p) of the virus. This protein has a sophisticated domain organization consisting of two N-terminal domains and one C-terminal domain, separated by flexible linkers. The molecular interactions between these domains and the known bacterial coreceptor protein (TolA) were studied using a biosensor technique, and we report here on interactions of the viral coat protein with TolA, as well as on interactions between the TolA molecules. We detected an interaction between the pilus binding second domain (N2) of protein 3 and the bacterial TolA. This novel interaction was found to depend on the periplasmatic domain of TolA... (More)
- The early events in filamentous bacteriophage infection of gram-negative bacteria are mediated by the gene 3 protein (g3p) of the virus. This protein has a sophisticated domain organization consisting of two N-terminal domains and one C-terminal domain, separated by flexible linkers. The molecular interactions between these domains and the known bacterial coreceptor protein (TolA) were studied using a biosensor technique, and we report here on interactions of the viral coat protein with TolA, as well as on interactions between the TolA molecules. We detected an interaction between the pilus binding second domain (N2) of protein 3 and the bacterial TolA. This novel interaction was found to depend on the periplasmatic domain of TolA (TolAII). Furthermore, extensive interaction was detected between TolA molecules, demonstrating that bacterial TolA has the ability to interact functionally with itself during phage infection. The kinetics of g3p binding to TolA is also different from that of bacteriocins, since both N-terminal domains of g3p were found to interact with TolA. The multiple roles for each of the separate g3p and TolA domains imply a delicate interaction network during the phage infection process and a model for the infection mechanism is hypothesized (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/131651
- author
- Karlsson, Fredrik LU ; Borrebaeck, Carl LU ; Nilsson, Nina and Malmborg Hager, Ann-Christin LU
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Bacteriology
- volume
- 185
- issue
- 8
- pages
- 2628 - 2634
- publisher
- American Society for Microbiology
- external identifiers
-
- pmid:12670988
- wos:000182068300027
- scopus:0037388018
- ISSN
- 0021-9193
- DOI
- 10.1128/JB.185.8.2628-2634.2003
- language
- English
- LU publication?
- yes
- id
- fa9ac8fa-6e14-4b89-8b41-f389e7f69114 (old id 131651)
- date added to LUP
- 2016-04-01 11:55:43
- date last changed
- 2022-02-03 07:08:34
@article{fa9ac8fa-6e14-4b89-8b41-f389e7f69114,
abstract = {{The early events in filamentous bacteriophage infection of gram-negative bacteria are mediated by the gene 3 protein (g3p) of the virus. This protein has a sophisticated domain organization consisting of two N-terminal domains and one C-terminal domain, separated by flexible linkers. The molecular interactions between these domains and the known bacterial coreceptor protein (TolA) were studied using a biosensor technique, and we report here on interactions of the viral coat protein with TolA, as well as on interactions between the TolA molecules. We detected an interaction between the pilus binding second domain (N2) of protein 3 and the bacterial TolA. This novel interaction was found to depend on the periplasmatic domain of TolA (TolAII). Furthermore, extensive interaction was detected between TolA molecules, demonstrating that bacterial TolA has the ability to interact functionally with itself during phage infection. The kinetics of g3p binding to TolA is also different from that of bacteriocins, since both N-terminal domains of g3p were found to interact with TolA. The multiple roles for each of the separate g3p and TolA domains imply a delicate interaction network during the phage infection process and a model for the infection mechanism is hypothesized}},
author = {{Karlsson, Fredrik and Borrebaeck, Carl and Nilsson, Nina and Malmborg Hager, Ann-Christin}},
issn = {{0021-9193}},
language = {{eng}},
number = {{8}},
pages = {{2628--2634}},
publisher = {{American Society for Microbiology}},
series = {{Journal of Bacteriology}},
title = {{The mechanism of bacterial infection by filamentous phages involves molecular interactions between TolA and phage protein 3 domains}},
url = {{https://lup.lub.lu.se/search/files/2706125/624240.pdf}},
doi = {{10.1128/JB.185.8.2628-2634.2003}},
volume = {{185}},
year = {{2003}},
}